EKS-MUM-00180
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-MUM-00180
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
AGC/PKC439.41.2E-131232486255
StatusReviewed
Ensembl ProteinENSMUSP00000107822
UniProt AccessionP28867; Q91V85; Q9Z333;
Protein NameProtein kinase C delta type
Protein Synonyms/Alias Tyrosine-protein kinase PRKCD; nPKC-delta;
Gene NamePrkcd
Gene Synonyms/Alias Prkcd; Pkcd;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSMUSG00000021948ENSMUSP00000107827ENSMUST00000112208
ENSMUSG00000021948ENSMUSP00000107825ENSMUST00000112206
ENSMUSG00000021948ENSMUSP00000107826ENSMUST00000112207
ENSMUSG00000021948ENSMUSP00000022521ENSMUST00000022521
ENSMUSG00000021948ENSMUSP00000107821ENSMUST00000112202
ENSMUSG00000021948ENSMUSP00000107822ENSMUST00000112203
ENSMUSG00000021948ENSMUSP00000107830ENSMUST00000112211
ENSMUSG00000021948ENSMUSP00000107829ENSMUST00000112210
OrganismMus musculus
Functional DescriptionCalcium-independent, phospholipid- and diacylglycerol(DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor- initiated cell death, is involved in tumor suppression, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Upon DNA damage, activates the promoter of the death- promoting transcription factor BCLAF1/Btf to trigger BCLAF1- mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl- leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C- terminal and regulates the interaction between MUC1 and beta- catenin.
Protein Length545
Protein Sequence
(FASTA)
MCVQYFLEDG DCKQSMRSEE EAKFPTMNRR GAIKQAKIHY IKNHEFIATF FGQPTFCSVC 60
KEFVWGLNKQ GYKCRQCNAA IHKKCIDKII GRCTGTATNS RDTIFQKERF NIDMPHRFKV 120
YNYMSPTFCD HCGSLLWGLV KQGLKCEDCG MNVHHKCREK VANLCGINQK LLAEALNQVT 180
QRSSRKLDTT ESVGIYQGFE KKPEVSGSDI LDNNGTYGKI WEGSTRCTLE NFTFQKVLGK 240
GSFGKVLLAE LKGKDKYFAI KCLKKDVVLI DDDVECTMVE KRVLALAWES PFLTHLICTF 300
QTKDHLFFVM EFLNGGDLMF HIQDKGRFEL YRATFYAAEI ICGLQFLHSK GIIYRDLKLD 360
NVMLDRDGHI KIADFGMCKE NIFGEGRAST FCGTPDYIAP EILQGLKYSF SVDWWSFGVL 420
LYEMLIGQSP FHGDDEDELF ESIRVDTPHY PRWITKESKD IMEKLFERDP DKRLGVTGNI 480
RIHPFFKTIN WSLLEKRKVE PPFKPKVQAC FLTPPGMLCM YHSLYSCILA ISALHSFRRQ 540
LELQI 545
Nucleotide Sequence
(FASTA)
ATGTGTGTGC AGTATTTCCT GGAGGATGGG GATTGCAAAC AGTCTATGCG TAGTGAGGAG 60
GAGGCAAAGT TTCCAACCAT GAACCGTCGT GGAGCCATTA AACAGGCCAA GATCCACTAC 120
ATCAAGAACC ACGAGTTTAT CGCCACCTTC TTCGGGCAGC CCACCTTCTG TTCTGTGTGC 180
AAAGAGTTTG TCTGGGGCCT CAACAAGCAA GGCTACAAAT GCAGGCAATG CAACGCTGCC 240
ATCCACAAGA AATGCATTGA CAAGATTATC GGCCGCTGCA CTGGCACTGC CACCAATAGC 300
CGGGACACCA TCTTCCAGAA AGAACGCTTC AACATCGACA TGCCTCACCG ATTCAAGGTT 360
TATAACTACA TGAGCCCCAC CTTCTGTGAC CACTGTGGCA GTTTGCTCTG GGGACTGGTG 420
AAGCAGGGAT TAAAGTGTGA AGATTGTGGC ATGAATGTGC ACCACAAATG CCGGGAGAAG 480
GTGGCCAACC TGTGTGGTAT CAACCAAAAG CTCTTGGCTG AGGCCTTGAA CCAAGTGACC 540
CAGAGATCTT CCCGGAAGCT GGACACAACA GAGTCTGTCG GAATATACCA GGGATTTGAG 600
AAGAAGCCAG AAGTCTCTGG GAGTGACATC CTAGACAACA ACGGGACCTA TGGCAAGATC 660
TGGGAGGGGA GCACCCGGTG CACCCTTGAG AACTTCACCT TCCAAAAAGT ACTTGGCAAA 720
GGCAGCTTTG GCAAGGTGCT GCTGGCAGAG CTGAAGGGCA AAGACAAGTA CTTTGCAATC 780
AAGTGTCTGA AGAAGGACGT GGTGTTGATT GACGATGATG TAGAGTGTAC CATGGTGGAG 840
AAGCGGGTGC TGGCGCTCGC CTGGGAGAGT CCCTTCCTCA CCCACCTCAT CTGTACCTTC 900
CAGACCAAGG ACCACCTGTT CTTCGTGATG GAGTTTCTCA ATGGGGGTGA CCTGATGTTC 960
CACATTCAGG ACAAAGGCCG CTTCGAACTC TACCGGGCTA CGTTTTATGC AGCTGAGATC 1020
ATCTGCGGAC TGCAGTTTCT ACACAGCAAA GGCATTATTT ACAGGGACCT CAAGCTGGAC 1080
AATGTGATGC TAGACAGGGA CGGCCACATC AAGATCGCTG ACTTTGGGAT GTGCAAAGAG 1140
AATATATTTG GGGAGGGCCG GGCCAGCACA TTCTGCGGCA CTCCTGACTA CATCGCCCCT 1200
GAGATCCTGC AGGGCCTGAA GTACTCCTTC TCGGTGGACT GGTGGTCTTT CGGGGTCCTC 1260
CTGTACGAAA TGCTCATCGG CCAGTCCCCC TTCCACGGCG ACGATGAGGA CGAGCTCTTC 1320
GAGTCCATCC GGGTGGACAC ACCACACTAT CCCCGTTGGA TCACCAAGGA ATCCAAGGAC 1380
ATCATGGAGA AGCTATTCGA GAGGGACCCT GACAAGAGGC TGGGAGTAAC AGGAAACATC 1440
AGGATTCACC CCTTTTTCAA GACTATCAAC TGGTCCCTCC TGGAGAAGCG GAAGGTGGAG 1500
CCGCCCTTTA AGCCCAAAGT GCAAGCCTGC TTCCTGACCC CTCCTGGCAT GCTGTGTATG 1560
TACCACAGCC TCTACTCTTG CATCCTCGCA ATCTCAGCCC TGCACTCATT CAGGAGACAG 1620
CTGGAACTGC AGATTTAG 1638
Domain Profile
S: 1     fellkvlGkGsfgkvllaelkktdelyaikvlkkdvvlqdddveltlvekrvlalaskkp  60
         f++ kvlGkGsfgkvllaelk++d+++aik+lkkdvvl dddve+t+vekrvlala+++p
Q: 232   FTFQKVLGKGSFGKVLLAELKGKDKYFAIKCLKKDVVLIDDDVECTMVEKRVLALAWESP  291
         89**********************************************************
S: 61    flvqlfscfqtedrlffvleyvnGGdlmfhiqkarklkeerarfyaaeiilalkflhekg  120
         fl++l+++fqt+d+lffv+e++nGGdlmfhiq++++++  ra+fyaaeii++l+flh+kg
Q: 292   FLTHLICTFQTKDHLFFVMEFLNGGDLMFHIQDKGRFELYRATFYAAEIICGLQFLHSKG  351
         ************************************************************
S: 121   iiyrdlkldnvlldaeGhikladfGlckeeilegkttstfcGtPdyiaPeilkeeeygks  180
         iiyrdlkldnv+ld++Ghik+adfG+cke+i+ + ++stfcGtPdyiaPeil++ +y++s
Q: 352   IIYRDLKLDNVMLDRDGHIKIADFGMCKENIFGEGRASTFCGTPDYIAPEILQGLKYSFS  411
         ************************************************************
S: 181   vdwwalGvllyemlagqsPfegededelfesilekevlyPkslskeaveilkglltkdpe  240
         vdww++Gvllyeml+gqsPf+g+dedelfesi+ ++++yP++++ke+++i+++l+++dp+
Q: 412   VDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDIMEKLFERDPD  471
         ************************************************************
S: 241   krlGvkeegeedikehaff  259
         krlGv  +g  +i+ h+ff
Q: 472   KRLGV--TG--NIRIHPFF  486
         *****..56..79999998
Domain Sequence
(FASTA)
FTFQKVLGKG SFGKVLLAEL KGKDKYFAIK CLKKDVVLID DDVECTMVEK RVLALAWESP 60
FLTHLICTFQ TKDHLFFVME FLNGGDLMFH IQDKGRFELY RATFYAAEII CGLQFLHSKG 120
IIYRDLKLDN VMLDRDGHIK IADFGMCKEN IFGEGRASTF CGTPDYIAPE ILQGLKYSFS 180
VDWWSFGVLL YEMLIGQSPF HGDDEDELFE SIRVDTPHYP RWITKESKDI MEKLFERDPD 240
KRLGVTGNIR IHPFF 255
Keyword3D-structure; Alternative splicing; Apoptosis; ATP-binding; Cell cycle; Complete proteome; Cytoplasm; Endoplasmic reticulum; Kinase; Membrane; Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase; Tumor suppressor; Zinc; Zinc-finger.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Equus caballus"; ?>Felis catus"; ?>Gorilla gorilla"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Monodelphis domestica"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Ochotona princeps"; ?>Oryctolagus cuniculus"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Petromyzon marinus"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>
EKS-AIM-00166
EKS-BOT-00176
EKS-CAJ-00179
EKS-CAF-00183
EKS-CAP-00173
EKS-EQC-00174
EKS-FEC-00164
EKS-GOG-00175
EKS-HOS-00182
EKS-ICT-00169
EKS-LOA-00173
EKS-MAM-00172
EKS-MOD-00172
EKS-MYL-00181
EKS-NOL-00169
EKS-OCP-00109
EKS-ORC-00160
EKS-OTG-00181
EKS-PAT-00166
EKS-PEM-00089
EKS-POA-00169
EKS-RAN-00172
EKS-SAH-00166
EKS-SUS-00150
Gene Ontology
GO:0005911; C:cell-cell junction
GO:0005829; C:cytosol
GO:0005783; C:endoplasmic reticulum
GO:0005739; C:mitochondrion
GO:0016363; C:nuclear matrix
GO:0048471; C:perinuclear region of cytoplasm
GO:0005886; C:plasma membrane
GO:0005524; F:ATP binding
GO:0008047; F:enzyme activator activity
GO:0046872; F:metal ion binding
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity
GO:0004697; F:protein kinase C activity
GO:0006915; P:apoptotic process
GO:0042100; P:B cell proliferation
GO:0007049; P:cell cycle
GO:0090398; P:cellular senescence
GO:0042742; P:defense response to bacterium
GO:0016064; P:immunoglobulin mediated immune response
GO:0032613; P:interleukin-10 production
GO:0032615; P:interleukin-12 production
GO:0035556; P:intracellular signal transduction
GO:0030837; P:negative regulation of actin filament polymerization
GO:0051490; P:negative regulation of filopodium assembly
GO:0034351; P:negative regulation of glial cell apoptotic process
GO:0046627; P:negative regulation of insulin receptor signaling pathway
GO:0043407; P:negative regulation of MAP kinase activity
GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation
GO:0090331; P:negative regulation of platelet aggregation
GO:0042119; P:neutrophil activation
GO:0018107; P:peptidyl-threonine phosphorylation
GO:2000304; P:positive regulation of ceramide biosynthetic process
GO:2000753; P:positive regulation of glucosylceramide catabolic process
GO:1900163; P:positive regulation of phospholipid scramblase activity
GO:0035307; P:positive regulation of protein dephosphorylation
GO:2001022; P:positive regulation of response to DNA damage stimulus
GO:2000755; P:positive regulation of sphingomyelin catabolic process
GO:0032930; P:positive regulation of superoxide anion generation
GO:0023021; P:termination of signal transduction
KEGG
mmu:18753;
InterPros
IPR000961; AGC-kinase_C.
IPR000008; C2_Ca-dep.
IPR008973; C2_Ca/lipid-bd_dom_CaLB.
IPR020454; DAG/PE-bd.
IPR011009; Kinase-like_dom.
IPR017892; Pkinase_C.
IPR014376; Prot_kin_PKC_delta.
IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
IPR000719; Prot_kinase_cat_dom.
IPR017441; Protein_kinase_ATP_BS.
IPR002290; Ser/Thr_dual-sp_kinase_dom.
IPR008271; Ser/Thr_kinase_AS.
Pfam
PF00130; C1_1; 2.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
SMARTs
SM00109; C1; 2.
SM00239; C2; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
Prosites
PS51285; AGC_KINASE_CTER; 1.
PS50004; C2; FALSE_NEG.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PS00479; ZF_DAG_PE_1; 2.
PS50081; ZF_DAG_PE_2; 2.
Prints
PR00008; DAGPEDOMAIN.
Created Date20-Feb-2013